Department of Chemistry, Yale University, New Haven, CT, USA.
Department of Chemistry, Yale University, New Haven, CT, USA; Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT, USA.
Curr Opin Struct Biol. 2017 Dec;47:123-130. doi: 10.1016/j.sbi.2017.08.002. Epub 2017 Sep 1.
Modern interpretations of allostery typically rely on conformational ensembles to describe enzyme function. Conformational motions controlling these ensembles are often stimulated or quenched by allosteric effectors, and are critical to optimizing ligand binding pockets and enzyme architectures. Thus, enzymes rely on dynamic allosteric pathways that transmit long-range binding information to control catalysis. In this review, we provide a brief discussion of the ever-expanding principles of allosteric regulation in enzyme catalysis and highlight in-depth studies of three enzymes that have contributed to the paradigms of dynamic allostery.
现代对变构作用的解释通常依赖于构象集合来描述酶的功能。控制这些集合的构象运动通常受到变构效应物的刺激或抑制，对于优化配体结合口袋和酶结构至关重要。因此，酶依赖于动态变构途径，将远程结合信息传递到控制催化。在这篇综述中，我们简要讨论了酶催化中变构调节的不断扩展的原则，并重点介绍了对动态变构范例有贡献的三种酶的深入研究。
